Recombinant-Saccharomyces-cere
visiae-Putative-uncharacterized-protein-YOR218CYOR218CPutative uncharacterized protein YOR218C- ￥10010
- CUSABIO
- CN
- CSB-CF615482SVG
- 2025年07月15日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
"-20°C/-80°C"
- 保质期：
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
- 英文名：
Customized Saccharomyces cerevisiae YOR218C Protein (in vitro E.coli)
- 库存：
200
- 供应商：
武汉华美生物工程有限公司
- 规格：
20ug
Alternative Name(s)
Putative uncharacterized protein YOR218CEditorial/Sponsord
EditorialUniprot ID
Q12249Gene Names
YOR218COrganism
Saccharomyces cerevisiaeAASequence
MNKSCFRFPFFATTRFTGGSLPLRRFGFLLDKFILLQVCATILCFFIICGNWIVICVNDI FEIGGASTGANTTTTNSTTCSVNCDWMCHTVVFPRESTFNRSWYLFDNGCGHIRTYEKLH NRIPVFFGQIVIVHYLYDRExpression Region
1-139aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1430Purity
Greater than 85% as determined by SDS-PAGE.Storage Buffer
Tris/PBS-based buffer, 6% TrehaloseStorage
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.Endotoxin
Not Test. Endotoxin removal service is available for free upon you request.产品类型
Transmembrane-Protein备注
**产品信息可能有变动，请以官网信息为准
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文献和实验**产品信息可能有变动，请以官网信息为准
Detection of Protein‐Protein Interactions by Coprecipitation
. Wang, Y., Chen, W., Simpson, D.M., and Elion, E.A. 2005. Cdc24 regulates nuclear shuttling and recruitment of the Ste5 scaffold to a heterotrimeric G protein in Saccharomyces cerevisiae. J. Biol. Chem. 280:1304‐13096
【资源】全面归类网址：毕赤酵母表达各种来源蛋白（细菌，真菌，植物，人类等）
316Saccharomyces cerevisiae Hsp70I, 21mg/g cells, active467Saccharomyces cerevisiae invertaseS, 2.5 g/L, native[86]Saccharomyces cerevisiaeKex 2pS, 100 mg/L, active458Saccharomyces cerevisiae Ktr1pS, 400 mg/L, PHO1[87]Saccharomyces cerevisiae (α
Secondary structure of prion mRNA
as the origin of the transformation of PrP C into PrP Sc is an attractive model (for review see Prusiner, 1994). It might be that putative structural elements in the PrP mRNA influence the kinetics of sequential folding of the protein during translation
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